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48-602MAG
Buffer Detection Kit for Magnetic Beads
1 Kit
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ABE30
Sigma-AldrichAnti-RNA polymerase II subunit B1 Antibody
Use Anti-RNA polymerase II subunit B1 Antibody, rabbit polyclonal antibody validated in WB, ICC to detect RNA polymerase II subunit B1 also known as DNA-directed RNA polymerase II subunit RPB1.
More>>Use Anti-RNA polymerase II subunit B1 Antibody, rabbit polyclonal antibody validated in WB, ICC to detect RNA polymerase II subunit B1 also known as DNA-directed RNA polymerase II subunit RPB1. Less<<
Anti-RNA polymerase II subunit B1 Antibody MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.
polymerase (RNA) II (DNA directed) polypeptide A, 220kDa
DNA-directed RNA polymerase III largest subunit
DNA-directed RNA polymerase II subunit RPB1
RNA polymerase II subunit B1
DNA-directed RNA polymerase II subunit A
DNA-directed RNA polymerase II largest subunit, RNA polymerase II 220 kd subunit
RNA-directed RNA polymerase II subunit RPB1
polymerase (RNA) II (DNA directed) polypeptide A (220kD)
Background Information
RNA polymerase II subunit B1 (RPB1) is the largest subunit of the RNA polymerase II complex. As a holoenzyme RNA polymerase II catalyzes transcription of eukaryotic DNA into RNA using the four ribonucleoside triphosphates as substrates. The RPB1 subunit, in combination with other polymerase subunits, forms a large central cleft that maintains contact between the active site of the enzyme, the DNA template, and the nascent RNA transcript. This subunit also contains a carboxy terminal domain (CTD) consisting of tandem heptapeptide repeats. In actively transcribing RNA polymerase ‘Ser-2’ and ‘Ser-5’ of the heptapeptide repeat are phosphorylated. Phosphorylation activates the RNA polymerase II beta subunit, allowing it to serve as an assembly platform for additional subunits that modulate initiation, elongation, termination and mRNA processing.
References
Product Information
Format
Affinity Purified
Control
HeLa nuclear extract
Presentation
Purified rabbit polyclonal in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.
Use Anti-RNA polymerase II subunit B1 Antibody, rabbit polyclonal antibody validated in WB, ICC to detect RNA polymerase II subunit B1 also known as DNA-directed RNA polymerase II subunit RPB1.
Key Applications
Western Blotting
Immunocytochemistry
Application Notes
Immunocytochemistry Analysis: 1:500 dilution from a representative lot detected RNA polymerase II subunit B1 in HeLa cells.
Biological Information
Immunogen
KLH-conjugated linear peptide corresponding to human RNA polymerase II subunit B1.
Concentration
Please refer to the Certificate of Analysis for the lot-specific concentration.
Host
Rabbit
Species Reactivity
Human
Mouse
Rat
Bovine
Horse
Canine
Species Reactivity Note
Demonstrated to react with Human. Predicted to react with Mouse, Rat, Bovine, Horse, and Canine based on 100% sequence homology.
Summary: This gene encodes the largest subunit of RNA polymerase II, the polymerase responsible for synthesizing messenger RNA in eukaryotes. The product of this gene contains a carboxy terminal domain composed of heptapeptide repeats that are essential for polymerase activity. These repeats contain serine and threonine residues that are phosphorylated in actively transcribing RNA polymerase. In addition, this subunit, in combination with several other polymerase subunits, forms the DNA binding domain of the polymerase, a groove in which the DNA template is transcribed into RNA. [provided by RefSeq].
FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Forms the polymerase active center together with the second largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB1 is part of the core element with the central large cleft, the clamp element that moves to open and close the cleft and the jaws that are thought to grab the incoming DNA template. At the start of transcription, a single stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol II. A bridging helix emanates from RPB1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol II by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition. During transcription elongation, Pol II moves on the template as the transcript elongates. Elongation is influenced by the phosphorylation status of the C-terminal domain (CTD) of Pol II largest subunit (RPB1), which serves as a platform for assembly of factors that regulate transcription initiation, elongation, termination and mRNA processing. Acts as a RNA-dependent RNA polymerase when associated with small delta antigen of Hepatitis delta virus, acting both as a replicate and transcriptase for the viral RNA circular genome.
SUBUNIT STRUCTURE: Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits. The phosphorylated C-terminal domain interacts with FNBP3 and SYNCRIP. Interacts with SAFB/SAFB1. Interacts with CCNL1 and MYO1C By similarity. Interacts with CCNL2 and SFRS19. Component of a complex which is at least composed of HTATSF1/Tat-SF1, the P-TEFb complex components CDK9 and CCNT1, RNA polymerase II, SUPT5H, and NCL/nucleolin. Interacts with PAF1. Interacts (via C-terminus) with FTSJD2, CTDSP1 and RBM16. Interacts via the phosphorylated C-terminal domain with WDR82 and with SETD1A and SETD1B only in the presence of WDR82.
SUBCELLULAR LOCATION: Nucleus.
POST-TRANSLATIONAL MODIFICATION: The tandem 7 residues repeats in the C-terminal domain (CTD) can be highly phosphorylated. The phosphorylation activates Pol II. Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5' of the heptapepdtide repeat. The phosphorylation state is believed to result from the balanced action of site-specific CTD kinases and phosphataes, and a "CTD code" that specifies the position of Pol II within the transcription cycle has been proposed. Dephosphorylated by the protein phosphatase CTDSP1.
Ubiquitinated by WWP2 leading to proteasomal degradation (by similarity).
MISCELLANEOUS: The binding of ribonucleoside triphosphate to the RNA polymerase II transcribing complex probably involves a two-step mechanism. The initial binding seems to occur at the entry (E) site and involves a magnesium ion temporarily coordinated by three conserved aspartate residues of the two largest RNA Pol II subunits. The ribonucleoside triphosphate is transferred by a rotation to the nucelotide addition (A) site for pairing with the template DNA. The catalytic A site involves three conserved aspartate residues of the RNA Pol II largest subunit which permanently coordinate a second magnesium ion.
SEQUENCE SIMILARITIES: Belongs to the RNA polymerase beta' chain family.
Molecular Weight
~217 kDa observed
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Quality Assurance
Evaluated by Western Blot in HeLa nuclear extract.
Western Blot Analysis: 1 µg/mL of this antibody detected RNA polymerase II subunit B1 on 10 µg of HeLa nuclear extract.
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Reduced RAN expression and disrupted transport between cytoplasm and nucleus; a key event in Alzheimer's disease pathophysiology. Mastroeni, D; Chouliaras, L; Grover, A; Liang, WS; Hauns, K; Rogers, J; Coleman, PD PloS one
8
e53349
2013
Transcription of DNA is essential for cell maintenance and survival; inappropriate localization of proteins that are involved in transcription would be catastrophic. In Alzheimer's disease brains, and in vitro studies, we have found qualitative and quantitative deficits in transport into the nucleus of DNA methyltransferase 1 (DNMT1) and RNA polymerase II (RNA pol II), accompanied by their abnormal sequestration in the cytoplasm. RAN (RAs-related Nuclear protein) knockdown, by siRNA and oligomeric Aβ42 treatment in neurons, replicate human data which indicate that transport disruption in AD may be mechanistically linked to reduced expression of RAN, a pivotal molecule in nucleocytoplasmic transport. In vitro studies also indicate a significant role for oligomeric Aβ42 in the observed phenomena. We propose a model in which reduced transcription regulators in the nucleus and their increased presence in the cytoplasm may lead to many of the cellular manifestations of Alzheimer's disease.
